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研究肝素酶 (来源于 Flavobacterum heparinase,EC4 .2 .2 .7)对人工合成的且含有与抗凝血酶 特定结合位点的肝素五糖 (SHP)的酶解作用 ,并对酶解作用的动力学进行研究。利用强阴离子高效液相色谱 (SAX- HPL C)对酶解混合物进行分离 ,利用质谱 (ESIMS)和核磁共振波谱 (1H- NMR)技术对得到的二糖和三糖的结构进行确证。研究结果表明 ,这种被作为肝素反向试剂的肝素酶 可水解人工所合成的肝素五糖 ,从而使之丧失抗 Xa因子活性。
Enzymolysis of heparinase (derived from Flavobacterum heparinase, EC4.2.2.7) on synthetic heparin pentasaccharide (SHP) containing a specific binding site for antithrombin was studied and the effect of enzymolysis The kinetics of the study. Enzymatic mixtures were separated using Strong Anion High Performance Liquid Chromatography (SAX-HPL C) and the structures of the disaccharides and trisaccharides obtained were confirmed by ESIMS and 1H-NMR techniques. The results show that this heparinase, which is used as a heparin reverse reagent, hydrolyzes artificially synthesized heparin pentasaccharide, thereby losing its anti-factor Xa activity.